Active protein and substrate flow effects in a tubular immobilized invertase reactor
✍ Scribed by F. N. Onyezili
- Publisher
- John Wiley and Sons
- Year
- 1991
- Tongue
- English
- Weight
- 398 KB
- Volume
- 11
- Category
- Article
- ISSN
- 0138-4988
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✦ Synopsis
Investigations of invertase (EC 3.2.1.26) immobilized inside modified nylon tubes showed that between 4% and 20% (w/w) of the protein exposed to binding sites on the tube was immobilized. An enhanced activity consistent with enzyme purification during immobilization was also evident, suggesting that, in scaled-up commercial applications, nylon tube invertase would be a more economical converter of sucrose than the free enzyme. The quantity and specific activity of the immobilized proteirt were not stoichiometrical with the amount used in the coupling solution and, in the system studied, a concentration of 2 mg ml-I was optimal.
K , and V,,, values confirmed higher rates of immobilized invertase catalysis when the rates of substrate flow through the reactor were higher. Higher rates of substrate flow imply a shortened residence time in the reactor and would lower the fractional conversion per pass of the substrate, reducing the efficiency of the reactor in flow-through situations. Thus, these higher catalysis rates, attributable a t the higher flow rates to a reduction of the diffusion barrier between enzyme and substrate, would not translate into improved economy in the commercial flow-through processes a t which the reactor is aimed.